Dual effect of Ca2+ on ultrasonic ATPase activity and polymerization of muscle actin

Millimolar concentrations of Ca2+ stimulate actin polymerization whereas micromolar concentrations of Ca2+ depress polymerization. This latter effect leads to a reduction of ATPase (ATP phosphohydrolase, EC 3.6.1.3) activity of actin during sonication at low Mg2+ concentrations and in the absence of KCl. In the presence of KCl (90 mM) there is activation of ATPase activity by micromolar Ca2+ concentrations. These Ca2+ effects are half-maximal at a Ca2+ concentration of 2-10(-7) M. They can be explained by assuming that that ATPase activity is optimal in a medium range of actin polymer stability and that micromolar Ca2+ concentrations tend to labilize and depolymerize F-actin.